MAMYB_ARATH
ID MAMYB_ARATH Reviewed; 309 AA.
AC Q9ASQ2; Q9FHJ4;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=Transcription factor MAMYB {ECO:0000305};
DE AltName: Full=Membrane-anchored MYB {ECO:0000303|PubMed:21477080};
GN Name=MAMYB {ECO:0000303|PubMed:21477080};
GN OrderedLocusNames=At5g45420 {ECO:0000312|Araport:AT5G45420};
GN ORFNames=MFC19.9 {ECO:0000312|EMBL:BAB09170.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND INDUCTION BY AUXIN.
RX PubMed=21477080; DOI=10.1111/j.1365-313x.2011.04602.x;
RA Slabaugh E., Held M., Brandizzi F.;
RT "Control of root hair development in Arabidopsis thaliana by an endoplasmic
RT reticulum anchored member of the R2R3-MYB transcription factor family.";
RL Plant J. 67:395-405(2011).
CC -!- FUNCTION: Transcription factor involved in the regulation of root hair
CC development, possibly through auxin signaling. Its endoplasmic
CC reticulum membrane localization is not compatible with its
CC transcription factor activity in the nucleus. May be cleaved to target
CC the nucleus. {ECO:0000269|PubMed:21477080}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21477080}; Multi-pass membrane protein
CC {ECO:0000255}. Nucleus {ECO:0000305|PubMed:21477080}. Note=Its
CC endoplasmic reticulum membrane localization is not compatible with its
CC transcription factor activity in the nucleus. May be cleaved to target
CC the nucleus. A truncated form of MAMYB (amino acids 84 to 309) lacking
CC the 2 transmembrane domains is localized to the nucleus.
CC {ECO:0000269|PubMed:21477080}.
CC -!- INDUCTION: Induced by auxin. {ECO:0000269|PubMed:21477080}.
CC -!- CAUTION: Its endoplasmic reticulum membrane localization is not
CC compatible with its transcription factor activity in the nucleus. May
CC be cleaved to target the nucleus. A truncated form of MAMYB (amino
CC acids 84 to 309) lacking the 2 transmembrane domains is localized to
CC the nucleus. {ECO:0000269|PubMed:21477080}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09170.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB018113; BAB09170.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95248.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69818.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69819.1; -; Genomic_DNA.
DR EMBL; AK117467; BAC42132.1; -; mRNA.
DR EMBL; AF367345; AAK32932.1; -; mRNA.
DR EMBL; AY074839; AAL69537.1; -; mRNA.
DR RefSeq; NP_001331471.1; NM_001344621.1.
DR RefSeq; NP_001331472.1; NM_001344620.1.
DR RefSeq; NP_568645.1; NM_123910.3.
DR AlphaFoldDB; Q9ASQ2; -.
DR IntAct; Q9ASQ2; 6.
DR STRING; 3702.AT5G45420.1; -.
DR iPTMnet; Q9ASQ2; -.
DR PaxDb; Q9ASQ2; -.
DR PRIDE; Q9ASQ2; -.
DR ProteomicsDB; 238874; -.
DR EnsemblPlants; AT5G45420.1; AT5G45420.1; AT5G45420.
DR EnsemblPlants; AT5G45420.2; AT5G45420.2; AT5G45420.
DR EnsemblPlants; AT5G45420.3; AT5G45420.3; AT5G45420.
DR GeneID; 834578; -.
DR Gramene; AT5G45420.1; AT5G45420.1; AT5G45420.
DR Gramene; AT5G45420.2; AT5G45420.2; AT5G45420.
DR Gramene; AT5G45420.3; AT5G45420.3; AT5G45420.
DR KEGG; ath:AT5G45420; -.
DR Araport; AT5G45420; -.
DR TAIR; locus:2163573; AT5G45420.
DR eggNOG; KOG0724; Eukaryota.
DR HOGENOM; CLU_077818_0_0_1; -.
DR InParanoid; Q9ASQ2; -.
DR OMA; RQMVKHP; -.
DR OrthoDB; 1392575at2759; -.
DR PRO; PR:Q9ASQ2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9ASQ2; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030544; F:Hsp70 protein binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IBA:GO_Central.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR CDD; cd00167; SANT; 2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR044634; Zuotin/DnaJC2.
DR PANTHER; PTHR43999; PTHR43999; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS50090; MYB_LIKE; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..309
FT /note="Transcription factor MAMYB"
FT /id="PRO_0000443061"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21477080"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..62
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:21477080"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21477080"
FT DOMAIN 156..209
FT /note="Myb-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT DOMAIN 244..298
FT /note="Myb-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 97..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 34363 MW; B1B3AA50DCB49898 CRC64;
MDFFDEDRPR FVFQSRPSSS HTAEEEEEAR IPNKLFISIS VSISLIILSL SFFYFESEPA
KSLLLWLSLS FLVGPFAPSS LTGGKIRVGY GQILEPEQIH DESSTDNERE SRRKSVNKRS
KGSTKSDNPP ENASAVTEVS RKVVIPQSKE SGSVNETKDW TAEEIEILKK QLIKHPAGKP
GRWETVASAF GGRYKTENVI KKAKEIGEKK IYESDDYAQF LKNRKASDPR LVDENEENSG
AGGDAEGTKE IWSNGEDIAL LNALKAFPKE AAMRWEKIAA AVPGKSKAAC MKRVTELKKG
FRSSKTPAN
